CDK7_CARAU
ID CDK7_CARAU Reviewed; 344 AA.
AC P51953;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cyclin-dependent kinase 7;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=40 kDa protein kinase;
DE AltName: Full=CDC2/CDK2,4-activating kinase;
DE AltName: Full=Cell division protein kinase 7;
DE AltName: Full=P40 MO15;
GN Name=cdk7; Synonyms=mo15;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RA Onoe S., Yamashita M., Kajiura H., Katsu Y., Jianquao J., Nagahama Y.;
RT "A fish homolog of the cdc2-related protein p40 MO15: its cDNA cloning and
RT expression in oocytes.";
RL Biomed. Res. 14:441-444(1993).
CC -!- FUNCTION: Serine/threonine kinase involved in cell cycle control and in
CC RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases
CC (CDKs) are activated by the binding to a cyclin and mediate the
CC progression through the cell cycle. Each different complex controls a
CC specific transition between 2 subsequent phases in the cell cycle.
CC Required for both activation and complex formation of cdk1/cyclin-B
CC during G2-M transition, and for activation of cdk2/cyclins during G1-S
CC transition (but not complex formation). cdk7 is the catalytic subunit
CC of the CDK-activating kinase (CAK) complex. CAK activates the cyclin-
CC associated kinases cdk1, cdk2, cdk4 and cdk6 by threonine
CC phosphorylation, thus regulating cell cycle progression. CAK complexed
CC to the core-TFIIH basal transcription factor activates RNA polymerase
CC II by serine phosphorylation of the repetitive C-terminal domain (CTD)
CC of its large subunit (polr2a), allowing its escape from the promoter
CC and elongation of the transcripts (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-169 is required for
CC enzymatic activity.
CC -!- SUBUNIT: Probably associates with cyclin-H (ccnh) and mat1 to form a
CC multimeric active enzyme. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylation of Ser-163 during mitosis inactivates the enzyme.
CC Phosphorylation of Thr-169 is required for activity. Phosphorylated at
CC Ser-163 and Thr-169 by CDK2 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; D38631; BAA07611.1; -; mRNA.
DR AlphaFoldDB; P51953; -.
DR SMR; P51953; -.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd07841; STKc_CDK7; 1.
DR InterPro; IPR037770; CDK7.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24056:SF375; PTHR24056:SF375; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Meiosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..344
FT /note="Cyclin-dependent kinase 7"
FT /id="PRO_0000085794"
FT DOMAIN 12..294
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 163
FT /note="Phosphoserine; by CDK1 and CDK2"
FT /evidence="ECO:0000250"
FT MOD_RES 169
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 344 AA; 38510 MW; 2AE835FFBEFAA1BA CRC64;
MALDVKSRAK LYEKLDFLGE GQFATVYKAR DKTTNTIVAI KKIKVGHRTE AKDGINRTAL
REIKLLQELS HPNIIGLLDA FGHKSNISLL CFMETDLEVI IKDTSLVLTP ANIKAYILMS
LQGLEYMHNH WILHRDLKPN NLLLDENGVL KLADFGLAKA FGSPNRVYTH QVVTRWYRAP
ELLFGARMYG VGVDMWAVGS ILAELLLRVP FLAGDSDLDQ LTGIFEALGT PTEETWPGMS
NLPDYVSFKL FPGTPLEHIF SAAGDDLLEL LKGLFTFNPC TRTTASQALK MRYFSIRPGP
TPGPQLPRPN SSTEALKEKE NLLIGIKRKR DSIEQGTLKK KLVF
